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Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem-apoprotein interactions

¹ Protein Structure Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100, Copenhagen, Denmark
² Dipartimento di Chimica, UniversitÁ di Firenze, Via G. Capponi 9, I-50121, Firenze, Italy
³ Department of Protein Chemistry, University of Copenhagen, Øster Farimagsgade 2A, DK-1353, København K, Denmark

Reprint requests to: Anette Henriksen, Carlsberg Laboratory, Department of Chemistry, Gamle Carlsberg Vej 10, DK-2500 Valby, Denmark; e-mail: anette{at}crc.dk; fax: ++45-33-27-47-08.

Soybean seed coat peroxidase (SBP) is a peroxidase with extraordinary stability and catalytic properties. It belongs to the family of class III plant peroxidases that can oxidize a wide variety of organic and inorganic substrates using hydrogen peroxide. Because the plant enzyme is a heterogeneous glycoprotein, SBP was produced recombinant in Escherichia coli for the present crystallographic study. The three-dimensional structure of SBP shows a bound tris(hydroxymethyl)aminomethane molecule (TRIS). This TRIS molecule has hydrogen bonds to active site residues corresponding to the residues that interact with the small phenolic substrate ferulic acid in the horseradish peroxidase C (HRPC):ferulic acid complex. TRIS is positioned in what has been described as a secondary substrate-binding site in HRPC, and the structure of the SBP:TRIS complex indicates that this secondary substrate-binding site could be of functional importance. SBP has one of the most solvent accessible -meso haem edge (the site of electron transfer from reducing substrates to the enzymatic intermediates compound I and II) so far described for a plant peroxidase and structural alignment suggests that the volume of Ile74 is a factor that influences the solvent accessibility of this important site. A contact between haem C8 vinyl and the sulphur atom of Met37 is observed in the SBP structure. This interaction might affect the stability of the haem group by stabilisation/delocalisation of the porphyrin -cation of compound I.

Keywords: Soybean peroxidase; crystal structure; thermal stability; active site interactions; haem accessibility; recombinant peroxidase

Abbreviations: ATP A2, Arabidopsis thaliana peroxidase A2 • ATP N, Arabidopsis thaliana peroxidase N • CCP, cytochrome c peroxidase • CIP, Coprinus cinereus peroxidase • FA, ferulic acid • HRPC, horseradish peroxidases C • HS, high spin • LIP, Lignin peroxidase • LS, low spin • PNP, peanut peroxidase • QS, quantum mechanically mixed-spin state • RR, resonance Raman • SBP, soybean peroxidase • TRIS, tris(hydroxymethyl)aminomethane.

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